2cfm: Difference between revisions
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Revision as of 18:02, 30 October 2007
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ATP-DEPENDENT DNA LIGASE FROM PYROCOCCUS FURIOSUS
OverviewOverview
DNA ligases join single-strand breaks in double-stranded DNA, and are, essential to maintain genome integrity in DNA metabolism. Here, we report, the 1.8 A resolution structure of Pyrococcus furiosus DNA ligase (PfuLig), which represents the first full-length atomic view of an ATP-dependent, eukaryotic-type DNA ligase. The enzyme comprises the N-terminal, DNA-binding domain, the middle adenylation domain, and the C-terminal, OB-fold domain. The architecture of each domain resembles those of human, DNA ligase I, but the domain arrangements differ strikingly between the, two enzymes. The closed conformation of the two "catalytic core" domains, at the carboxyl terminus in PfuLig creates a small compartment, which, holds a non-covalently bound AMP molecule. This domain rearrangement, results ... [(full description)]
About this StructureAbout this Structure
2CFM is a [Single protein] structure of sequence from [Pyrococcus furiosus] with MG and AMP as [ligands]. Active as [DNA ligase (ATP)], with EC number [6.5.1.1]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
The closed structure of an archaeal DNA ligase from Pyrococcus furiosus., Nishida H, Kiyonari S, Ishino Y, Morikawa K, J Mol Biol. 2006 Jul 28;360(5):956-67. Epub 2006 Jun 12. PMID:16820169
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